Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase. 1991

J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
Unité de Biologie Moléculaire, Institut des Biotechnologies, Vitry-sur-Seine, France.

A 13.1-kb DNA fragment carrying Pseudomonas denitrificans cob genes has been sequenced. The nucleotide sequence and genetic analysis revealed that this fragment contained five different cob genes named cobN to cobQ and cobW. Based on the similarity of NH2-terminal sequences and molecular weights of the purified Cob proteins, CobQ was identified as cobyric acid synthase, CobP was identified as a bifunctional enzyme exhibiting both cobinamide kinase and cobinamide phosphate guanylyltransferase activities, and CobO was identified as cob(I)alamin adenosyltransferase. CobN is proposed to play a role in cobalt insertion reactions. Four other open reading frames were identified on the 13.1-kb fragment, but their chromosomal inactivation did not lead to a cobalamin-minus phenotype.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D009713 Nucleotidyltransferases A class of enzymes that transfers nucleotidyl residues. EC 2.7.7. Nucleotidyltransferase
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D011549 Pseudomonas A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants. Chryseomonas,Pseudomona,Flavimonas
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D005816 Genetic Complementation Test A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell. Allelism Test,Cis Test,Cis-Trans Test,Complementation Test,Trans Test,Allelism Tests,Cis Tests,Cis Trans Test,Cis-Trans Tests,Complementation Test, Genetic,Complementation Tests,Complementation Tests, Genetic,Genetic Complementation Tests,Trans Tests
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
October 1990, Journal of bacteriology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
October 1991, Journal of bacteriology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
October 1991, Journal of bacteriology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
October 1991, Journal of bacteriology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
October 1990, Journal of bacteriology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
March 1984, The Journal of biological chemistry,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
September 1988, Nucleic acids research,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
November 1994, Applied and environmental microbiology,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
May 1981, The Journal of biological chemistry,
J Crouzet, and S Levy-Schil, and B Cameron, and L Cauchois, and S Rigault, and M C Rouyez, and F Blanche, and L Debussche, and D Thibaut
January 1991, Journal of bacteriology,
Copied contents to your clipboard!